CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004312
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Lysyl-tRNA synthetase; LysRS 
Gene Name
 KRS1 
Gene Synonyms/Alias
 GCD5; YDR037W; YD9673.09 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
29ATGEMVSKSELKKRIacetylation[1]
86RQIQELRKTHEPNPYubiquitination[2]
123GETLPEEKVSIAGRIacetylation[1]
241YLDLIMNKDARNRFIubiquitination[2]
265RRFLDQRKFIEVETPubiquitination[2]
284IAGGATAKPFITHHNubiquitination[2]
308IAPELFLKQLVVGGLubiquitination[2, 3]
375ITGSYIIKYHPDPADacetylation[1]
411LEKVFNVKFPSGDQLacetylation[1]
428AETGEFLKKILVDNKacetylation[1]
435KKILVDNKLECPPPLubiquitination[2]
450TNARMLDKLVGELEDubiquitination[2]
577VLLFPTLKPDVLREEacetylation[1]
577VLLFPTLKPDVLREEubiquitination[2, 3]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
  
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 30 30 Phosphoserine.
 MOD_RES 62 62 Phosphothreonine.  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 591 AA 
Protein Sequence
MSQQDNVKAA AEGVANLHLD EATGEMVSKS ELKKRIKQRQ VEAKKAAKKA AAQPKPASKK 60
KTDLFADLDP SQYFETRSRQ IQELRKTHEP NPYPHKFHVS ISNPEFLAKY AHLKKGETLP 120
EEKVSIAGRI HAKRESGSKL KFYVLHGDGV EVQLMSQLQD YCDPDSYEKD HDLLKRGDIV 180
GVEGYVGRTQ PKKGGEGEVS VFVSRVQLLT PCLHMLPADH FGFKDQETRY RKRYLDLIMN 240
KDARNRFITR SEIIRYIRRF LDQRKFIEVE TPMMNVIAGG ATAKPFITHH NDLDMDMYMR 300
IAPELFLKQL VVGGLDRVYE IGRQFRNEGI DMTHNPEFTT CEFYQAYADV YDLMDMTELM 360
FSEMVKEITG SYIIKYHPDP ADPAKELELN FSRPWKRINM IEELEKVFNV KFPSGDQLHT 420
AETGEFLKKI LVDNKLECPP PLTNARMLDK LVGELEDTCI NPTFIFGHPQ MMSPLAKYSR 480
DQPGLCERFE VFVATKEICN AYTELNDPFD QRARFEEQAR QKDQGDDEAQ LVDETFCNAL 540
EYGLPPTGGW GCGIDRLAMF LTDSNTIREV LLFPTLKPDV LREEVKKEEE N 591 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004824; F:lysine-tRNA ligase activity; IDA:SGD.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006430; P:lysyl-tRNA aminoacylation; IDA:SGD. 
Interpro
 IPR004364; aa-tRNA-synt_II.
 IPR018150; aa-tRNA-synt_II-like.
 IPR006195; aa-tRNA-synth_II.
 IPR002313; Lys-tRNA-ligase_II.
 IPR018149; Lys-tRNA-synth_II_C.
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase. 
Pfam
 PF00152; tRNA-synt_2
 PF01336; tRNA_anti 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR00982; TRNASYNTHLYS.